Structure of PDB 3fcl Chain A

Receptor sequence
>3fclA (length=222) Species: 9606 (Homo sapiens) [Search protein sequence]
EFFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMC
DIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIE
DFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSW
LNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCR
HFSKTNELLQKSGKKPIDWKEL
3D structure
PDB3fcl Impact of linker strain and flexibility in the design of a fragment-based inhibitor
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D145 Y147 F158 H268
Catalytic site (residue number reindexed from 1) D63 Y65 F76 H186
Enzyme Commision number 3.2.2.27: uracil-DNA glycosylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 3FL A G143 Q144 D145 Y147 C157 F158 N204 H268 S270 S273 G61 Q62 D63 Y65 C75 F76 N122 H186 S188 S191 MOAD: ic50=315uM
PDBbind-CN: -logKd/Ki=3.50,IC50=315uM
BindingDB: IC50=3.15e+5nM
Gene Ontology
Molecular Function
GO:0004844 uracil DNA N-glycosylase activity
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3fcl, PDBe:3fcl, PDBj:3fcl
PDBsum3fcl
PubMed19396178
UniProtP13051|UNG_HUMAN Uracil-DNA glycosylase (Gene Name=UNG)

[Back to BioLiP]